[English] 日本語
Yorodumi
- PDB-3ll1: Monomeric Griffithsin with a Single Gly-Ser Insertion and Mutatio... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 3ll1
TitleMonomeric Griffithsin with a Single Gly-Ser Insertion and Mutations to Remove Residual Self-Association
ComponentsGriffithsin
KeywordsSUGAR BINDING PROTEIN / lectin / sugar-binding / anti-HIV / high mannose / Man9 / gp120 / gp41 / jacalin-related / Mannose-binding
Function / homology
Function and homology information


N-acetylgalactosamine binding / D-glucose binding / D-mannose binding / carbohydrate binding / identical protein binding
Similarity search - Function
Jacalin-like lectin domain / Jacalin-like lectin domain / Jacalin-type lectin domain profile. / Aligned Prism / Vitelline Membrane Outer Layer Protein I, subunit A / Jacalin-like lectin domain / Jacalin-like lectin domain / Jacalin-like lectin domain superfamily / Mainly Beta
Similarity search - Domain/homology
Biological speciesGriffithsia (eukaryote)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 0.97 Å
AuthorsMoulaei, T. / Wlodawer, A.
CitationJournal: Structure / Year: 2010
Title: Monomerization of viral entry inhibitor griffithsin elucidates the relationship between multivalent binding to carbohydrates and anti-HIV activity.
Authors: Moulaei, T. / Shenoy, S.R. / Giomarelli, B. / Thomas, C. / McMahon, J.B. / Dauter, Z. / O'Keefe, B.R. / Wlodawer, A.
History
DepositionJan 28, 2010Deposition site: RCSB / Processing site: RCSB
Revision 1.0Oct 6, 2010Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Nov 1, 2017Group: Refinement description / Category: software
Revision 1.3Oct 13, 2021Group: Database references / Derived calculations / Category: database_2 / struct_ref_seq_dif / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 1.4Sep 6, 2023Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Griffithsin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)12,6632
Polymers12,6281
Non-polymers351
Water2,486138
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)55.4, 55.4, 61.8
Angle α, β, γ (deg.)90, 90, 120
Int Tables number152
Space group name H-MP3121

-
Components

#1: Protein Griffithsin / GRFT


Mass: 12627.627 Da / Num. of mol.: 1
Mutation: Gly-Ser insertion after S16, L2S, E119D, Q120N, deltaY121
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Griffithsia (eukaryote) / Strain: Q66D336 / Plasmid: pET-15b / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P84801
#2: Chemical ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Cl
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 138 / Source method: isolated from a natural source / Formula: H2O

-
Experimental details

-
Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

-
Sample preparation

CrystalDensity Matthews: 2.17 Å3/Da / Density % sol: 43.27 %
Crystal growTemperature: 298 K / Method: vapor diffusion, sitting drop / pH: 3.5
Details: 0.1M citric acid, 3M NaCl, pH 3.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 22-ID / Wavelength: 1 Å
DetectorType: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Apr 3, 2009
RadiationMonochromator: Si(220) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 0.97→50 Å / Num. obs: 65427 / % possible obs: 99.9 % / Redundancy: 7.1 % / Rmerge(I) obs: 0.082 / Χ2: 1.45 / Net I/σ(I): 13.3
Reflection shellResolution: 0.97→1 Å / Redundancy: 5.2 % / Rmerge(I) obs: 0.78 / Mean I/σ(I) obs: 2 / Num. unique all: 6418 / Χ2: 0.935 / % possible all: 99.4

-
Phasing

Phasing MRRfactor: 46.61 / Model details: Phaser MODE: MR_AUTO
Highest resolutionLowest resolution
Rotation2.5 Å27.7 Å
Translation2.5 Å27.7 Å

-
Processing

Software
NameVersionClassificationNB
DENZOdata reduction
SCALEPACKdata scaling
PHASER2.1.3phasing
REFMACrefinement
PDB_EXTRACT3.005data extraction
HKL-3000data collection
HKL-3000data reduction
HKL-3000data scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 3LKY

3lky


Resolution: 0.97→30 Å / Cor.coef. Fo:Fc: 0.977 / Cor.coef. Fo:Fc free: 0.971 / WRfactor Rfree: 0.165 / WRfactor Rwork: 0.152 / Occupancy max: 1 / Occupancy min: 0.33 / FOM work R set: 0.92 / SU B: 0.49 / SU ML: 0.014 / SU R Cruickshank DPI: 0.022 / SU Rfree: 0.022 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.022 / ESU R Free: 0.022 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.165 976 1.5 %RANDOM
Rwork0.152 ---
obs0.152 -99.95 %-
all-65253 --
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso max: 52.42 Å2 / Biso mean: 14.177 Å2 / Biso min: 7.51 Å2
Baniso -1Baniso -2Baniso -3
1--0.32 Å2-0.16 Å20 Å2
2---0.32 Å20 Å2
3---0.48 Å2
Refinement stepCycle: LAST / Resolution: 0.97→30 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms888 0 1 138 1027
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0180.0211044
X-RAY DIFFRACTIONr_bond_other_d0.0020.02700
X-RAY DIFFRACTIONr_angle_refined_deg2.3041.951415
X-RAY DIFFRACTIONr_angle_other_deg1.32231704
X-RAY DIFFRACTIONr_dihedral_angle_1_deg7.8985143
X-RAY DIFFRACTIONr_dihedral_angle_2_deg34.35923.25643
X-RAY DIFFRACTIONr_dihedral_angle_3_deg12.45715159
X-RAY DIFFRACTIONr_dihedral_angle_4_deg20.308156
X-RAY DIFFRACTIONr_chiral_restr0.1330.2148
X-RAY DIFFRACTIONr_gen_planes_refined0.0120.021243
X-RAY DIFFRACTIONr_gen_planes_other0.0050.02231
X-RAY DIFFRACTIONr_nbd_refined0.2090.2198
X-RAY DIFFRACTIONr_nbd_other0.2120.2701
X-RAY DIFFRACTIONr_nbtor_refined0.190.2508
X-RAY DIFFRACTIONr_nbtor_other0.1050.2581
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.2540.2101
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.2420.218
X-RAY DIFFRACTIONr_symmetry_vdw_other0.3270.255
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.2730.224
X-RAY DIFFRACTIONr_mcbond_it2.1651.5848
X-RAY DIFFRACTIONr_mcbond_other1.3581.5305
X-RAY DIFFRACTIONr_mcangle_it2.66921090
X-RAY DIFFRACTIONr_scbond_it3.7073422
X-RAY DIFFRACTIONr_scangle_it4.7044.5325
X-RAY DIFFRACTIONr_rigid_bond_restr1.81431270
X-RAY DIFFRACTIONr_sphericity_bonded4.81831020
LS refinement shellResolution: 0.97→0.995 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.201 79 -
Rwork0.259 4645 -
all-4724 -
obs--99.41 %

+
About Yorodumi

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242)：Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi

Thousand views of thousand structures

  • Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
  • This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
  • The word "yorodu" (or yorozu) is an old Japanese word meaning "ten thousand". "mi" (miru) is to see.

Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi

Read more